ArticleOpen biology2016
Combined structural, biochemical and cellular evidence demonstrates that both FGDF motifs in alphavirus nsP3 are required for efficient replication.
Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- Alphavirus nsP3 as a multifunctional orchestrator of virus-host interplay.Journal of virology · 2026Review
- AI-discovered protein fragments as generalizable regulators of biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
- Innate immune sensing of alphavirus chikungunya: balancing antiviral defense and pathogenesis.Frontiers in immunology · 2026Review
- Pharmacological modulation of stress granulesFrontiers in pharmacology · 2026Review
- The SHFV nsp2 and nucleocapsid proteins recruit G3BP1 to sites of viral replication, but stress granules are not induced by the infection.Journal of virology · 2025Article
- Article
- Convergent evolution of the G3BP1-binding motif in betacoronavirus nucleocapsid proteins.Virus evolution · 2025Article
- SARS-CoV-2 N protein recruits G3BP to double membrane vesicles to promote translation of viral mRNAs.Nature communications · 2024Article
- G3BP isoforms differentially affect stress granule assembly and gene expression during cellular stress.Molecular biology of the cell · 2024Article
- Enhancement of Stress Granule Formation by a Chiral Compound Targeting G3BP1 via eIF2α Phosphorylation.International journal of molecular sciences · 2024Article
- Stress granule formation helps to mitigate neurodegeneration.Nucleic acids research · 2024Article
- Article
- TRIM25 predominately associates with anti-viral stress granules.Nature communications · 2024Article
- Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication and pathogenicity.Cell reports · 2024Article
- Identification of small molecule inhibitors of G3BP-driven stress granule formation.The Journal of cell biology · 2024Article
- Stress granule formation helps to mitigate neurodegeneration.bioRxiv : the preprint server for biology · 2023Article
- Role(s) of G3BPs in Human Pathogenesis.The Journal of pharmacology and experimental therapeutics · 2023Review
- Caprin-1 binding to the critical stress granule protein G3BP1 is influenced by pH.Open biology · 2023Article
- Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs.Nature communications · 2023Article
- Identification of mosquito proteins that differentially interact with alphavirus nonstructural protein 3, a determinant of vector specificity.PLoS neglected tropical diseases · 2023Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent findings have highlighted the role of the Old World alphavirus non-structural protein 3 (nsP3) as a host defence modulator that functions by disrupting stress granules, subcellular phase-dense RNA/protein structures formed upon environmental stress. This disruption mechanism was largely explained through nsP3-mediated recruitment of the host G3BP protein via two tandem FGDF motifs. Here, we present the 1.9 Å resolution crystal structure of the NTF2-like domain of G3BP-1 in complex with a 25-residue peptide derived from Semliki Forest virus nsP3 (nsP3-25). The structure reveals a poly-complex of G3BP-1 dimers interconnected through the FGDF motifs in nsP3-25. Although in vitro and in vivo binding studies revealed a hierarchical interaction of the two FGDF motifs with G3BP-1, viral growth curves clearly demonstrated that two intact FGDF motifs are required for efficient viral replication. Chikungunya virus nsP3 also binds G3BP dimers via a hierarchical interaction, which was found to be critical for viral replication. These results highlight a conserved molecular mechanism in host cell modulation.
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